ID A0A223NWP3_9SPHI Unreviewed; 1069 AA.
AC A0A223NWP3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE AltName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273};
GN ORFNames=MuYL_2321 {ECO:0000313|EMBL:ASU34210.1};
OS Mucilaginibacter xinganensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1234841 {ECO:0000313|EMBL:ASU34210.1, ECO:0000313|Proteomes:UP000215002};
RN [1] {ECO:0000313|EMBL:ASU34210.1, ECO:0000313|Proteomes:UP000215002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJC16-A31 {ECO:0000313|EMBL:ASU34210.1,
RC ECO:0000313|Proteomes:UP000215002};
RG Henan University of Science and Technology;
RA You X.;
RT "Complete genome sequence of Mucilaginibacter sp. strain BJC16-A31.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|ARBA:ARBA00007391}.
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DR EMBL; CP022743; ASU34210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223NWP3; -.
DR KEGG; muc:MuYL_2321; -.
DR Proteomes; UP000215002; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07434; PHP_PolIIIA_DnaE2; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01902; DNApol_error_prone; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR023073; DnaE2.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF4; ERROR-PRONE DNA POLYMERASE; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000215002};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..81
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1069 AA; 121005 MW; 0B146C72C07A95FB CRC64;
MDSLHEKGVK MSYIELQVTT NFSFLRGGAH PEELVTQAAD YGQVKIAITD RNSVAGVVRA
HIAAKAREMK IIPACRLDLL DGPSLLAYPT DQEAWGRLCG ILTTGNLRAE KGECYLYKQD
VYTQAKGMKF MAVPPAALNK QFDFDDSFKI ALNEYREVFG RELYLAASKS YNGDDAKRLY
RLSRLGVPMV ATNDVYYHEP ARRELQDVLT CVREKRTIQN AGFLLHPNAE RHLKPSAEMK
RLFRQYPDAT GLTLEIAEAC TFSLDTLKYI EPEEISPDGL TPQERLTRFT WEGARKRFGA
DVPERIKEQI EFELEFIGRK NLASYFLRVY RYTRKAEELN ILYQGRGSAA NSTVCYCLAI
TAVNPMKSRL LFSRFMSDAR DEWPDIDVDF EHERREEIIQ FIYEDYGRER AAIVATVTQE
RHKGAIRDVG KAMELSEDTI KRLSGAIWHF SEEAFDRQRI LEQGLNPDDP QLRKVLELTE
QLMGFPRQLG QHTGGFVITR GKLSDICPVM NARMENRTQL EWNKDDLEAL SILKVDVLGL
GMLTCIRKGF ELAKQHYELD LTLANIPQDD PAVYEMICHA DTLGVFQIES RAQMSMLPRL
KPRCFYDLVI EVAIVRPGPI QGDMVHPYLR RRDGIDPVEY PSKELEEILG RTLGVPLFQE
QAMEIAIVAA GFTPAEADQL RRSMATFKAK GLVSQHRKKL VDGMMKKGYA EDFANRIFKQ
LEGFGSYGFP ESHAASFAHL VYVSSWLKWH YPDVFAAALL NSQPMGFYQP AQIVIDAERH
EVTVRPVDIN NSMWDNTLEE KTGKYFAVRL GFRQVKGLAE DDIQALIVAR GKGYTSISQL
SDAGVSQAAI ERLTDADAFR SLKLDRREAL WEVPALSDKP VGLFAGQPSE SNYEAQITLP
FMTQAEHVVQ DYASTGLSLK AHPVSFVREK LRLLHVTATG ELANMKDGDP VKVAGLVTVR
QRPGTAKGIL FITIEDETGF SNLVVWEKVF ETHRKEILQA RLLMVEGKLQ IEGEVIHVIV
KRCFNLSALL RGLTATENEN LPVLTLSRSD ETTSPAPVKE VFHKGRNFR
//
